Abstract
The crystal structure of RhoA bound an effector domain of protein kinase N has been determined at 2.2 Å resolution. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, strands B2 and B3, and C-terminal helix A5, predominantly by specific hydrogen bonds. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.
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